ID   FAEC_NEOFI              Reviewed;         272 AA.
AC   A1DI08;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Probable feruloyl esterase C;
DE            EC=3.1.1.73;
DE   AltName: Full=Ferulic acid esterase C;
DE   Flags: Precursor;
GN   Name=faeC; ORFNames=NFIA_089720;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- FUNCTION: Involved in degradation of plant cell walls. Hydrolyzes the
CC       feruloyl-arabinose ester bond in arabinoxylans, and the feruloyl-
CC       galactose ester bond in pectin. Active against paranitrophenyl-acetate,
CC       methyl ferulate and wheat arabinoxylan (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=feruloyl-polysaccharide + H2O = ferulate + polysaccharide.;
CC         EC=3.1.1.73;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the faeC family. {ECO:0000305}.
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DR   EMBL; DS027696; EAW19015.1; -; Genomic_DNA.
DR   RefSeq; XP_001260912.1; XM_001260911.1.
DR   AlphaFoldDB; A1DI08; -.
DR   SMR; A1DI08; -.
DR   STRING; 331117.A1DI08; -.
DR   ESTHER; neofi-faec; FaeC.
DR   EnsemblFungi; EAW19015; EAW19015; NFIA_089720.
DR   GeneID; 4587470; -.
DR   KEGG; nfi:NFIA_089720; -.
DR   VEuPathDB; FungiDB:NFIA_089720; -.
DR   eggNOG; ENOG502SMEI; Eukaryota.
DR   HOGENOM; CLU_027551_2_0_1; -.
DR   OMA; SSGCGKQ; -.
DR   OrthoDB; 1257904at2759; -.
DR   Proteomes; UP000006702; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030600; F:feruloyl esterase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR043595; FaeB/C/D.
DR   InterPro; IPR034429; FaeC.
DR   PANTHER; PTHR38050; PTHR38050; 1.
DR   PANTHER; PTHR38050:SF1; PTHR38050:SF1; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Hydrolase; Polysaccharide degradation;
KW   Reference proteome; Secreted; Serine esterase; Signal; Xylan degradation.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..272
FT                   /note="Probable feruloyl esterase C"
FT                   /id="PRO_0000394943"
SQ   SEQUENCE   272 AA;  28757 MW;  8E8F4BF97CA5741B CRC64;
     MVPTMIYSAI LALSAFTPSV LAQTRSSGCG KQPSLTNGVH NINGREYILK VPDNYDKNKA
     HHLVFGLHWR GGNMWNIVDG QSVQPWYGLE TRAQGSTIFV APNGKNAGWA NNGGEDIAFI
     DAIIKQVEGD LCVDQSSRFA TGFSWGGGMS YSLACSRAKQ FRAVSVLSGG VISGCDGGND
     PIAYLGIHGI NDGVLPFQGG VNLAQKFVKN NRCQQANVGT PQPGSHGSVR TDFKGCSKPV
     SFIAYDGGHD AAPLGVGSSL APDATWKFFM AA